National Institutes of Health, U.S.

Human serum transferrin crystal structure clarifies receptor binding

Published in Genetics and Environmental Business Week, October 19th, 2006

According to recent research from the United States, the crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding.

"Serum transferrin reversibly binds iron in each of two lobes and delivers it to cells by a receptor-mediated, pH-dependent process. The binding and release of iron result in a large conformational change in which two subdomains in each lobe close or open with a rigid twisting motion around a hinge," wrote J. Wally and colleagues, National Institute of Diabetes & Digestive & Kidney Diseases.

"We report the structure of human serum transferrin (hTF) lacking iron (apo-hTF),...

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Source: Genetics and Environmental Business Week (2006-10-19)

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